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Background
Aromatase cytochrome P450, Cholesterol 7-alpha-monooxygenase, is protein that plays a vital part in the regulation the ovarian sex cycle and other reproductive functions through the production of estrogen from androgens. . As a member of the Cytochrome P450 family, this protein is classified as monooxygenases. Members of this family act throughout the body to both catalyze and synthesize a multitude of reactions.

Structure
Aromatase is located on chromosome 15q21.1 in humans and has two ligands. The first is Protopophyrin IX containing iron and the second is an unknown atom or molecule.

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This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids. This protein localizes to the endoplasmic reticulum and catalyzes the last steps of estrogen biosynthesis from androgens. These steps include three successive hydroxylations of the 19-methyl group of androgens followed by simultaneous elimination of the methyl group as formate and aromatization of the A-ring. Mutations in this gene can result in either increased or decreased aromatase activity; the associated phenotypes suggest that estrogen functions both as a sex steroid hormone and in growth or differentiation.

This synthesis occurs in various tissues through tissue-specific regulatory factors. The regulation of aromatase is tissue-specific and acts through suppression and inductive processes. In the majority of tissues, aromatase is activated by cAMP or factors that use cAMP as a secondary messenger. In adipose tissues aromatase is induced by dexamethasone and phorbol ester which is suppressed by TGFß. aromatase through tissue-specific regulatory factorsIL-6 is produced by various types of lymphoid and non-lymphoid cells, such as T cells, B cells, monocytes, fibroblasts, kerationcytes, endothelial cells, mesangium cells, and several tumor cells.